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J Bacteriol. 1987 August; 169(8): 3861–3865.
PMCID: PMC212484

Uptake of cell wall peptides by Salmonella typhimurium and Escherichia coli.


During bacterial growth, cell wall peptides are released from the murein and reused for the synthesis of new cell wall material. Mutants defective in peptide transport were unable to reutilize cell wall peptides, demonstrating that these peptides are taken up intact into the cytoplasm prior to reincorporation into murein. Furthermore, cell wall peptide recycling was shown to play an important physiological role; peptide transport mutants which were unable to recycle these peptides showed growth defects under appropriate conditions. Using mutants specifically defective in each of the three peptide transport systems, we showed that the uptake of cell wall peptides was mediated solely by the oligopeptide permease (Opp) and that neither the dipeptide permease (Dpp) nor the tripeptide permease (Tpp) played a significant role in this process. Our data indicate that the periplasmic oligopeptide-binding protein has more than one substrate-binding site, each with different though overlapping specificities.

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Selected References

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  • Gibson MM, Ellis EM, Graeme-Cook KA, Higgins CF. OmpR and EnvZ are pleiotropic regulatory proteins: positive regulation of the tripeptide permease (tppB) of Salmonella typhimurium. Mol Gen Genet. 1987 Apr;207(1):120–129. [PubMed]
  • Gibson MM, Price M, Higgins CF. Genetic characterization and molecular cloning of the tripeptide permease (tpp) genes of Salmonella typhimurium. J Bacteriol. 1984 Oct;160(1):122–130. [PMC free article] [PubMed]
  • Goodell EW. Recycling of murein by Escherichia coli. J Bacteriol. 1985 Jul;163(1):305–310. [PMC free article] [PubMed]
  • Goodell EW, Schwarz U. Release of cell wall peptides into culture medium by exponentially growing Escherichia coli. J Bacteriol. 1985 Apr;162(1):391–397. [PMC free article] [PubMed]
  • Guyer CA, Morgan DG, Staros JV. Binding specificity of the periplasmic oligopeptide-binding protein from Escherichia coli. J Bacteriol. 1986 Nov;168(2):775–779. [PMC free article] [PubMed]
  • Helmstetter CE. DNA synthesis during the division cycle of rapidly growing Escherichia coli B/r. J Mol Biol. 1968 Feb 14;31(3):507–518. [PubMed]
  • Higgins CF, Gibson MM. Peptide transport in bacteria. Methods Enzymol. 1986;125:365–377. [PubMed]
  • Higgins CF, Hardie MM. Periplasmic protein associated with the oligopeptide permeases of Salmonella typhimurium and Escherichia coli. J Bacteriol. 1983 Sep;155(3):1434–1438. [PMC free article] [PubMed]
  • Higgins CF, Hardie MM, Jamieson D, Powell LM. Genetic map of the opp (Oligopeptide permease) locus of Salmonella typhimurium. J Bacteriol. 1983 Feb;153(2):830–836. [PMC free article] [PubMed]
  • Hiles ID, Gallagher MP, Jamieson DJ, Higgins CF. Molecular characterization of the oligopeptide permease of Salmonella typhimurium. J Mol Biol. 1987 May 5;195(1):125–142. [PubMed]
  • Hiles ID, Higgins CF. Peptide uptake by Salmonella typhimurium. The periplasmic oligopeptide-binding protein. Eur J Biochem. 1986 Aug 1;158(3):561–567. [PubMed]
  • Hiles ID, Powell LM, Higgins CF. Peptide transport in Salmonella typhimurium: molecular cloning and characterization of the oligopeptide permease genes. Mol Gen Genet. 1987 Jan;206(1):101–109. [PubMed]
  • Jamieson DJ, Higgins CF. Anaerobic and leucine-dependent expression of a peptide transport gene in Salmonella typhimurium. J Bacteriol. 1984 Oct;160(1):131–136. [PMC free article] [PubMed]
  • Jamieson DJ, Higgins CF. Two genetically distinct pathways for transcriptional regulation of anaerobic gene expression in Salmonella typhimurium. J Bacteriol. 1986 Oct;168(1):389–397. [PMC free article] [PubMed]
  • Leive L, Davis BD. The transport of diaminopimelate and cystine in Escherichia coli. J Biol Chem. 1965 Nov;240(11):4362–4369. [PubMed]
  • Manson MD, Blank V, Brade G, Higgins CF. Peptide chemotaxis in E. coli involves the Tap signal transducer and the dipeptide permease. Nature. 1986 May 15;321(6067):253–256. [PubMed]
  • Payne JW, Bell G. Direct determination of the properties of peptide transport systems in Escherichia coli, using a fluorescent-labeling procedure. J Bacteriol. 1979 Jan;137(1):447–455. [PMC free article] [PubMed]
  • Payne JW, Morley JS, Armitage P, Payne GM. Transport and hydrolysis of antibacterial peptide analogues in Escherichia coli: backbone-modified aminoxy peptides. J Gen Microbiol. 1984 Sep;130(9):2253–2265. [PubMed]
  • Schwarz U, Asmus A, Frank H. Autolytic enzymes and cell division of Escherichia coli. J Mol Biol. 1969 May 14;41(3):419–429. [PubMed]
  • Siewert G, Strominger JL. Biosynthesis of the peptidoglycan of bacterial cell walls. XI. Formation of the isoglutamine amide group in the cell walls of Staphylococcus aureus. J Biol Chem. 1968 Feb 25;243(4):783–790. [PubMed]
  • WORK E. Reaction of ninhydrin in acid solution with straight-chain amino acids containing two amino groups and its application to the estimation of alpha epsilon-diaminopimelic acid. Biochem J. 1957 Nov;67(3):416–423. [PubMed]

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